ID   ABL_FSVHY               Reviewed;         439 AA.
AC   P10447;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Abl;
DE            EC=2.7.10.2;
DE   AltName: Full=V-abl;
GN   Name=ABL;
OS   Feline sarcoma virus (strain Hardy-Zuckerman 2).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11776;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3029415; DOI=10.1128/jvi.61.4.1193-1202.1987;
RA   Bergold P.J., Blumenthal J.A., D'Andrea E., Snyder H.W. Jr., Lederman L.,
RA   Silverstone A., Nguyen H., Besmer P.;
RT   "Nucleic acid sequence and oncogenic properties of the HZ2 feline sarcoma
RT   virus v-abl insert.";
RL   J. Virol. 61:1193-1202(1987).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Abl-Pol
CC       polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M15805; AAA43042.1; -; mRNA.
DR   PIR; A26132; A26132.
DR   BMRB; P10447; -.
DR   SMR; P10447; -.
DR   BRENDA; 2.7.10.2; 2234.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007154; P:cell communication; IEA:UniProt.
DR   GO; GO:0023052; P:signaling; IEA:UniProt.
DR   CDD; cd09935; SH2_ABL; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR033221; ABL1.
DR   InterPro; IPR035837; ABL_SH2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418:SF162; PTHR24418:SF162; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..439
FT                   /note="Tyrosine-protein kinase transforming protein Abl"
FT                   /id="PRO_0000088056"
FT   DOMAIN          10..70
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          76..166
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          191..439
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           330..354
FT                   /note="Kinase activation loop"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         197..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         265..271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   439 AA;  50005 MW;  13579EDFED1481AB CRC64;
     ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE AQTKNGQGWV
     PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR SISLRYEGRV
     YHYRINTASD GKLYVSPESR FNTLAELVHH HSTVADGLIT TLHYPAPKRN KPTVYGVSPN
     YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE EFLKEAAVMK
     EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVNAVVLL YMATQISSAM
     EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGTKF PIKWTAPESL
     AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP EGCPEKVYEL
     MRACWQWNPS DRPAFAEIH